Purification and characterization of β-agarase from seaweed decomposing bacterium Microbulbifer sp. Strain CMC-5

Jonnadula, RaviChand; Ghadi, Sanjeev C.

doi:10.1007/s12257-010-0399-y

Cited by 27 publications

(12 citation statements)

References 32 publications

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“…The figure shows that there is a slow decrease of anzyme activity at a temperature of 20-40 O C, then increase very sharp at 50 O C and decline at 60 o C. Optimum activity of agarase enzyme isolated from Hypocreaceae sp. occurs at temperature of 50 O C. So that maximum activity of agarase enzyme was obtained at a temperature of 50 O C. Jonnadula and Ghadi (2011) stated that the average marine microorganisms has agarase activity at the optimum temperature range of 30-50 O C at intervals of 5 O C. Optimum agarase enzyme activity produced by B. cereus (Suzuki et al, 2002), B. megaterium (Khambhaty et al, 2008), and Acinetobacter sp. (Lakshmikanth et al, 2006) are all at a temperature between 30-50 O C. Temperatures can affect the enzyme activity since increased temperatures can accelerate a reaction.…”

Section: Acid and Temperature Characteristicsmentioning

confidence: 99%

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Potential Marine Fungi Hypocreaceae sp. as Agarase Enzyme to Hydrolyze Macroalgae Gelidium latifolium (Potensi Jamur Hypocreaceae sp. sebagai Enzim Agarase untuk menghidrolisis Makroalga Gelidium latifolium)

et al. 2015

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Agarase dapat mendegradasi agar ke oligosakarida dan memiliki banyak manfaat untuk makanan, kosmetik, dan lain-lain. Banyak spesies pendegradasi agar adalah organismelaut. Beberapa agarase telah diisolasi dari genera yang berbeda dari mikroorganisme yang ditemukan di air dan sedimen laut. Hypocreaceae sp. diisolasi dari air laut Pulau Pari, Kepulauan Seribu, Jakarta, Indonesia. Berdasarkan hasil identifikasi gen 16S rDNA dari 500 basis pasangan, isolat A10 memiliki 99% kesamaan dengan Hypocreaceae sp. Enzim agarase ekstraseluler dari Hypocreaceae sp. memiliki pH dan suhu optimum pada 8 TrisHCl (0,148 μ.mL-1) dan 50°C (0,182 μ.mL-1), masing-masing. Enzim Agarase dari Hypocreaceae sp. mencapai kondisi optimum pada aktivitas enzim tertinggi selama inkubasi dalam 24 jam (0,323 μ.mL-1). SDS page mengungkapkan bahwa ada dua band dari protein yang dihasilkan oleh agarase dari Hypocreaceae sp. yang berada di berat molekul 39 kDa dan 44 kDa dan hidrolisis Gelidium latifolium diperoleh 0,88% etanol. Kata kunci: enzim agarase, Hypocreaceae sp., hidrolisis, fungi, rDNA. Agarase can degradedagarto oligosaccharide and has a lot of benefits for food, cosmetics, and others. Many species of agar- degrader are marine-organism. Several agarases have been isolated from different genera of microorganisms found in seawater and marine sediments. Hypocreaceae sp. was isolated from sea water of Pari Islands, Seribu Islands, Jakarta, Indonesia. Based on the results of the 16S rDNA gene identification of 500 base pairs, A10 isolates had 99 % similarity toHypocreaceae sp. The extracellular agarase enzyme from Hypocreaceae sp. have optimum pH and temperature at 8 TrisHCl (0.148 µ.mL-1) and 50 °C (0.182 µ.mL-1), respectively. Agarase enzyme of Hypocreaceae sp. reach an optimum condition at the highest enzyme activity during incubation in 24 hours (0.323 µ.mL-1). SDS Page revealed that there are two bands of protein produced by agarase of Hypocreaceae sp. which are at molecular weight of 39 kDa and 44 kDa and hydrolisis of Gelidium latifolium obtained 0,88% ethanol. Key words: agarase enzym, Hypocreaceae sp., hydrolysis, marine fungi, rDNA

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Section: Acid and Temperature Characteristicsmentioning

confidence: 99%

“…(Aoki et al, 1990). Based on molecular weight classification agarase enzyme it was known that agarase produced by S. cucurbitacearum is included in the classification 2 (≤50 kDa) (Jonnadula and Ghadi, 2011).…”

Section: Molecular Weight (Sds Page)mentioning

confidence: 99%

Potential Marine Fungi Hypocreaceae sp. as Agarase Enzyme to Hydrolyze Macroalgae Gelidium latifolium (Potensi Jamur Hypocreaceae sp. sebagai Enzim Agarase untuk menghidrolisis Makroalga Gelidium latifolium)

et al. 2015

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“…LQ48 has been observed to be 52 kDa [17], and that of AgaA from Zobellia sp. has been found to be 69 kDa [10]; all of these agarases belong to Group II β-agarases. In the present study, the molecular mass of agarase BI-3 was found to be 58 kDa, suggesting that the enzyme belongs to Group II β-agarases.…”

Section: Separation and Identification Of Agarase Bi-3mentioning

confidence: 99%

Purification and Characterization of Thermostable Agarase from Bacillus sp. BI-3, a Thermophilic Bacterium Isolated from Hot Spring

Li¹,

Sha²,

Zilda³

et al. 2014

Journal of Microbiology and Biotechnology

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An extracellular agarase was purified from Bacillus sp. BI-3, a thermophilic agar-degrading bacterium isolated from a hot spring in Indonesia. The purified agarase revealed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with an apparent molecular mass of 58 kDa. The optimum pH and temperature of the agarase were 6.4 and 70°C, respectively. The activity of the agarase was stable at high temperatures, and more than 50% activity was retained at 80°C for 15 min. Furthermore, the enzyme was stable in the pH range of 5.8-8.0, and more than 60% of the residual activity was retained. Significant activation of the agarase was observed in the presence of K(+), Na(+), Ca(2+), Mg(2+), and Sr(2+); on the other hand, Ba(2+), Zn(2+), Cu(2+), Mn(2+), Co(2+), Fe(2+), and EDTA inhibited or inactivated the enzyme activity. The components of the hydrolytic product analyzed by thin-layer chromatography showed that the agarase mainly produced neoagarobiose. This study is the first to present evidence of agarolytic activity in aerobic thermophilic bacteria.

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“…Many agarolytic bacteria have been identified from seawater, marine algae, and marine sediments, including Agarivorans (Fu, Lin, & Kim, 2008;Lin et al, 2012), Alteromonas (Potin et al, 1993), Catenovulum (Cui, Dong, Shi, Zhao, & Zhang, 2014), Cytophaga (Duckworth & Turvey, 1969), Flammeovirga (Hou, Chen, Chan, & Zeng, 2015;Yang et al, 2011), Microbulbifer (Jonnadula & Ghadi, 2011;Miyazaki et al, 2008;Ohta et al, 2004), Microscilla (Naganuma, Coury, Polne-Fuller, Gibor, & Horikoshi, 1993;Zhong et al, 2001), Paenibacillus (Mei et al, 2014), Pseudoalteromonas (Chi, Park, Kang, & Hong, 2014;Lu et al, 2009;Oh et al, 2010;Vera, Alvarez, Murano, Slebe, & Leon, 1998;Xavier Chiura & Kita-Tsukamoto, 2000), Pseudomonas (Belas, Bartlett, & Silverman, 1988;Morrice, McLean, Williamson, & Long, 1983), Pseudozobellia (Nedashkovskaya et al, 2009), Saccharophagus (Ekborg et al, 2006), Vibrio (Sugano et al, 1993;Zhang & Sun, 2007), and Zobellia (Jam et al, 2005). These agarolytic bacteria metabolize agar primarily with β-agarase.…”

mentioning

confidence: 99%

Agarolytic bacteriumPersicobactersp. CCB-QB2 exhibited a diauxic growth involving galactose utilization pathway

et al. 2016

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The agarolytic bacterium Persicobacter sp. CCB‐QB2 was isolated from seaweed (genus Ulva) collected from a coastal area of Malaysia. Here, we report a high‐quality draft genome sequence for QB2. The Rapid Annotation using Subsystem Technology (RAST) annotation server identified four β‐agarases (PdAgaA, PdAgaB, PdAgaC, and PdAgaD) as well as galK, galE, and phosphoglucomutase, which are related to the Leloir pathway. Interestingly, QB2 exhibited a diauxic growth in the presence of two kinds of nutrients, such as tryptone and agar. In cells grown with agar, the profiles of agarase activity and growth rate were very similar. galK, galE, and phosphoglucomutase genes were highly expressed in the second growth phase of diauxic growth, indicating that QB2 cells use galactose hydrolyzed from agar by its agarases and exhibit nutrient prioritization. This is the first report describing diauxic growth for agarolytic bacteria. QB2 is a potential novel model organism for studying diauxic growth in environmental bacteria.

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Purification and characterization of β-agarase from seaweed decomposing bacterium Microbulbifer sp. Strain CMC-5

Cited by 27 publications

References 32 publications

Potential Marine Fungi Hypocreaceae sp. as Agarase Enzyme to Hydrolyze Macroalgae Gelidium latifolium (Potensi Jamur Hypocreaceae sp. sebagai Enzim Agarase untuk menghidrolisis Makroalga Gelidium latifolium)

Potential Marine Fungi Hypocreaceae sp. as Agarase Enzyme to Hydrolyze Macroalgae Gelidium latifolium (Potensi Jamur Hypocreaceae sp. sebagai Enzim Agarase untuk menghidrolisis Makroalga Gelidium latifolium)

Purification and Characterization of Thermostable Agarase from Bacillus sp. BI-3, a Thermophilic Bacterium Isolated from Hot Spring

Agarolytic bacteriumPersicobactersp. CCB-QB2 exhibited a diauxic growth involving galactose utilization pathway

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